Kaspaza-5

Kaspaza-5
Identifikatori
EC broj 3.4.22.58
CAS broj 192465-11-5
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC articles
PubMed articles
NCBI Protein search

Kaspaza-5 (EC 3.4.22.58, ICErel-III, Ich-3, ICH-3 proteaza, transkript Y, TY, CASP-5) je enzim.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju

Neophodno je prisustvo Asp ostatka u P1 poziciji. Preferentno dolazi do razlaganja sekvence Tyr-Val-Ala-Asp- ali se takođe razlaže Asp-Glu-Val-Asp-

Ovaj enzim pripada familiji inflamatornih kaspaza, koja takođe obuhvata kaspazu-1 (EC 3.4.22.36) i kaspazu-4 (EC 3.4.22.57) kod ljudi i kaspazu-11 (EC 3.4.22.64), kaspazu-12, kaspazu-13 i kaspazu-14 kod miševa.

Reference

  1. Faucheu, C., Blanchet, A.M., Collard-Dutilleul, V., Lalanne, J.L. and Diu-Hercend, A. (1996). „Identification of a cysteine protease closely related to interleukin-1 β-converting enzyme”. Eur. J. Biochem. 236: 207-213. PMID 8617266. 
  2. Kamada, S., Funahashi, Y. and Tsujimoto, Y. (1997). „Caspase-4 and caspase-5, members of the ICE/CED-3 family of cysteine proteases, are CrmA-inhibitable proteases”. Cell Death Differ. 4: 473-478. PMID 16465268. 
  3. Lin, X.Y., Choi, M.S. and Porter, A.G. (2000). „Expression analysis of the human caspase-1 subfamily reveals specific regulation of the CASP5 gene by lipopolysaccharide and interferon-γ”. J. Biol. Chem. 275: 39920-39926. PMID 10986288. 
  4. Fassy, F., Krebs, O., Rey, H., Komara, B., Gillard, C., Capdevila, C., Yea, C., Faucheu, C., Blanchet, A.M., Miossec, C. and Diu-Hercend, A. (1998). „Enzymatic activity of two caspases related to interleukin-1β-converting enzyme”. Eur. J. Biochem. 253: 76-83. PMID 9578463. 
  5. Martinon, F. and Tschopp, J. (2004). „Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases”. Cell 117: 561-574. PMID 15163405. 
  6. Chang, H.Y. and Yang, X. (2000). „Proteases for cell suicide: functions and regulation of caspases”. Microbiol. Mol. Biol. Rev. 64: 821-846. PMID 11104820. 

Literatura

  • Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. 
  • Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. 
  • Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. 
  • Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. 
  • Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. 

Spoljašnje veze

  • p
  • r
  • u
TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6